Implications of a high dielectric constant in proteins
Lund, Mikael LU
; Jönsson, Bo
LU
and Woodward, Clifford
(2007)
In Journal of Chemical Physics
126(22).
- Abstract
- Solvation of protein surface charges plays an important role for the protonation states of titratable surface groups and is routinely incorporated in low dielectric protein models using surface accessible areas. For many-body protein simulations, however, such dielectric boundary methods are rarely tractable and a greater level of simplification is desirable. In this work, we scrutinize how charges on a high dielectric surface are affected by the nonpolar interior core of the protein. A simple dielectric model, which models the interior as a low dielectric sphere, combined with Monte Carlo simulations, shows that for small, hydrophilic proteins the effect of the low dielectric interior is largely negligible and that the protein (and... (More)
- Solvation of protein surface charges plays an important role for the protonation states of titratable surface groups and is routinely incorporated in low dielectric protein models using surface accessible areas. For many-body protein simulations, however, such dielectric boundary methods are rarely tractable and a greater level of simplification is desirable. In this work, we scrutinize how charges on a high dielectric surface are affected by the nonpolar interior core of the protein. A simple dielectric model, which models the interior as a low dielectric sphere, combined with Monte Carlo simulations, shows that for small, hydrophilic proteins the effect of the low dielectric interior is largely negligible and that the protein (and solution) can be approximated with a uniform high dielectric constant equal to that of the solvent. This is verified by estimates of titration curves and acidity constants for four different proteins (BPTI, calbindin D-9k, ribonuclease A, and turkey ovomucoid third domain) that all correlate well with experimental data. Furthermore, the high dielectric approximation follows as a natural consequence of the multipole expansion of the potential due to embedded protein charges in the presence of the low dielectric core region. (c) 2007 American Institute of Physics. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/648827
- author
- Lund, Mikael
LU
; Jönsson, Bo
LU
and Woodward, Clifford
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chemical Physics
- volume
- 126
- issue
- 22
- publisher
- American Institute of Physics (AIP)
- external identifiers
-
- wos:000247247400048
- scopus:34250702227
- ISSN
- 0021-9606
- DOI
- 10.1063/1.2741543
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- e448def7-55e1-43ed-92db-b9f9bf7ffd7e (old id 648827)
- date added to LUP
- 2016-04-01 11:45:24
- date last changed
- 2023-01-02 22:57:09
@article{e448def7-55e1-43ed-92db-b9f9bf7ffd7e,
abstract = {{Solvation of protein surface charges plays an important role for the protonation states of titratable surface groups and is routinely incorporated in low dielectric protein models using surface accessible areas. For many-body protein simulations, however, such dielectric boundary methods are rarely tractable and a greater level of simplification is desirable. In this work, we scrutinize how charges on a high dielectric surface are affected by the nonpolar interior core of the protein. A simple dielectric model, which models the interior as a low dielectric sphere, combined with Monte Carlo simulations, shows that for small, hydrophilic proteins the effect of the low dielectric interior is largely negligible and that the protein (and solution) can be approximated with a uniform high dielectric constant equal to that of the solvent. This is verified by estimates of titration curves and acidity constants for four different proteins (BPTI, calbindin D-9k, ribonuclease A, and turkey ovomucoid third domain) that all correlate well with experimental data. Furthermore, the high dielectric approximation follows as a natural consequence of the multipole expansion of the potential due to embedded protein charges in the presence of the low dielectric core region. (c) 2007 American Institute of Physics.}},
author = {{Lund, Mikael and Jönsson, Bo and Woodward, Clifford}},
issn = {{0021-9606}},
language = {{eng}},
number = {{22}},
publisher = {{American Institute of Physics (AIP)}},
series = {{Journal of Chemical Physics}},
title = {{Implications of a high dielectric constant in proteins}},
url = {{http://dx.doi.org/10.1063/1.2741543}},
doi = {{10.1063/1.2741543}},
volume = {{126}},
year = {{2007}},
}